Structure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism

Here we determined the structure of a cold active family IV esterase (EstN7) cloned from Bacillus cohnii strain N1. EstN7 is a dimer with a classical α/β hydrolase fold. It has an acidic surface that is thought to play a role in cold-adaption by retaining solvation under changed water solvent entrop...

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Detalles Bibliográficos
Autores principales: Noby, Nehad, Auhim, Husam Sabah, Winter, Samuel, Worthy, Harley L., Embaby, Amira M., Saeed, Hesham, Hussein, Ahmed, Pudney, Christopher R., Rizkallah, Pierre J., Wells, Stephen A., Jones, D. Dafydd
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society 2021
Materias:
Research
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8633780/
https://www.ncbi.nlm.nih.gov/pubmed/34847772
http://dx.doi.org/10.1098/rsob.210182

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8633780/
https://www.ncbi.nlm.nih.gov/pubmed/34847772
http://dx.doi.org/10.1098/rsob.210182

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